Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter

Journal of Biological Chemistry

Volumn 282, Issue 43, 2007, Pages 31380-31388

  Ran, Yanchao ^a   Zhu, Hui ^a   Liu, Mengyao ^a   Fabian, Marian ^b   Olson, John S ^b   Aranda IV, Roman ^c   Phillips Jr , George N ^d   Dooley, David M ^a   Lei, Benfang ^a  

^a MONTANA STATE UNIVERSITY   (United States)

^b RICE UNIVERSITY   (United States)

^c UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

^d UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; MOLECULAR BIOLOGY; MUTAGENESIS;

KINETIC PHASES; LIGATION; LIPOPROTEINS; TRANSPORTER ACTIVE SITES;

PROTEINS;

ABC TRANSPORTER; ALANINE; CELL SURFACE PROTEIN; HEME; HEMIN; HEMOPROTEIN; METHIONINE; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTOPORPHYRIN; SCATTER FACTOR RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; CELL SURFACE; CONTROLLED STUDY; CRYSTALLIZATION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SHIGELLA DYSENTERIAE; STREPTOCOCCUS EQUI; STREPTOCOCCUS PYOGENES;

ALANINE; AMINO ACID SUBSTITUTION; ATP-BINDING CASSETTE TRANSPORTERS; BINDING SITES; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HEMIN; HYDROGEN-ION CONCENTRATION; KINETICS; MEMBRANE PROTEINS; METHIONINE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STREPTOCOCCUS PYOGENES;

STREPTOCOCCUS PYOGENES;

EID: 35748969327     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M705967200     Document Type: Article

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